Eukaryotic protein trafficking involves the packaging of molecules into membranous vesicles that bud from a donor compartment, travel to a specific destination, fuse, and release their components into an acceptor compartment. Recognition between vesicle and acceptor membrane is mediated by the pairing of the integral membrane SNARE proteins. The stable interaction between vesicle proteins (v-SNAREs) and target proteins (t-SNAREs) juxtaposes the membranes and results in an activated docking state and/or membrane fusion. The syntaxin protein family contains a number of members that serve as functional t-SNAREs. One member of this family, syntaxin 8, has two coiled-coil domains, one in the N-terminus and one toward the C-terminus. The C-terminal domain is homologous to a similar domain in syntaxin 6 and is predicted to interact in the formation of SNARE complexes, while a hydrophobic domain in the C-terminus may be involved in membrane anchoring. Syntaxin-8 is ubiquitously expressed, but is present at high levels in the heart and localizes specifically to the ER. Thus, syntaxin-8 is a t-SNARE that is thought to be involved in the early secretory pathway of many different cell types.